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Kinetic and energetic constraints on electron transfer in photosystem II
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Gates, Colin. Kinetic and energetic constraints on electron transfer in photosystem II. Retrieved from https://doi.org/doi:10.7282/t3-b7b6-2n84

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TitleKinetic and energetic constraints on electron transfer in photosystem II
NameGates, Colin (author); Dismukes, G. Charles (chair); Khare, Sagar (internal member); Falkowski, Paul (internal member); Bhattacharya, Debashish (outside member); Rutgers University; School of Graduate Studies
Date Created2018
Other Date2018-10 (degree)
SubjectChemistry and Chemical Biology, Photosystem II
Extent1 online resource (199 pages) : illustrations
DescriptionThe enzyme supercomplex Photosystem II (PSII) is the sole water oxidase known to have developed in nature. Accordingly, it is the source of almost all biologically useful reductant present in the biosphere, as well as the molecular oxygen in Earth’s atmosphere. Understanding this massive, complex protein is thus crucial to development of novel bioinspired water-oxidizing catalysts, a crucial step toward reducing dependence on fossil fuels, which are also ultimately products of PSII activity. Improving understanding and control of the operation and regulation of PSII is also critical for development of agriculture, biofuels, and bioproducts.
As the active domains of PSII are highly conserved, substitution of functional and tuning components of the complex and investigation of alterations to functionality represents a well-proven method for study of this complex. However, the development of a range of novel techniques for phenomenological investigation of PSII has allowed for the observation of previously unknown processes and functionalities associated with certain components of PSII. The use of exogenous quinones to remove the kinetic constraint of electron removal from the acceptor side of PSII allows a more accurate determination of the first electron transfer steps within PSII, removing a major confounding variable from kinetic studies of processes within the enzyme. Expansion of fluorometric and oximetric techniques allows processes to be probed under conditions previously inaccessible due to the need to generate specific and often unnatural sample conditions. With these new developments, cofactor substitutions are employed to clarify the functionality of the native cofactors.
NotePh.D.
NoteIncludes bibliographical references
Noteby Colin Gates
Genretheses, ETD doctoral
Persistent URLhttps://doi.org/doi:10.7282/t3-b7b6-2n84
Languageeng
CollectionSchool of Graduate Studies Electronic Theses and Dissertations
Organization NameRutgers, The State University of New Jersey
RightsThe author owns the copyright to this work.
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